ID B8IKT9_METNO Unreviewed; 233 AA.
AC B8IKT9;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE RecName: Full=Phosphoglycolate phosphatase {ECO:0000256|ARBA:ARBA00013078, ECO:0000256|HAMAP-Rule:MF_00495};
DE Short=PGP {ECO:0000256|HAMAP-Rule:MF_00495};
DE Short=PGPase {ECO:0000256|HAMAP-Rule:MF_00495};
DE EC=3.1.3.18 {ECO:0000256|ARBA:ARBA00013078, ECO:0000256|HAMAP-Rule:MF_00495};
GN Name=gph {ECO:0000256|HAMAP-Rule:MF_00495};
GN OrderedLocusNames=Mnod_1296 {ECO:0000313|EMBL:ACL56296.1};
OS Methylobacterium nodulans (strain LMG 21967 / CNCM I-2342 / ORS 2060).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Methylobacteriaceae; Methylobacterium.
OX NCBI_TaxID=460265 {ECO:0000313|EMBL:ACL56296.1, ECO:0000313|Proteomes:UP000008207};
RN [1] {ECO:0000313|EMBL:ACL56296.1, ECO:0000313|Proteomes:UP000008207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 21967 / CNCM I-2342 / ORS 2060
RC {ECO:0000313|Proteomes:UP000008207};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Marx C.J.,
RA Richardson P.;
RT "Complete sequence of chromosome of Methylobacterium nodulans ORS 2060.";
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Specifically catalyzes the dephosphorylation of 2-
CC phosphoglycolate. Is involved in the dissimilation of the intracellular
CC 2-phosphoglycolate formed during the DNA repair of 3'-phosphoglycolate
CC ends, a major class of DNA lesions induced by oxidative stress.
CC {ECO:0000256|HAMAP-Rule:MF_00495}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-phosphoglycolate + H2O = glycolate + phosphate;
CC Xref=Rhea:RHEA:14369, ChEBI:CHEBI:15377, ChEBI:CHEBI:29805,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58033; EC=3.1.3.18;
CC Evidence={ECO:0000256|ARBA:ARBA00000830, ECO:0000256|HAMAP-
CC Rule:MF_00495};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|HAMAP-Rule:MF_00495};
CC -!- PATHWAY: Organic acid metabolism; glycolate biosynthesis; glycolate
CC from 2-phosphoglycolate: step 1/1. {ECO:0000256|ARBA:ARBA00004818,
CC ECO:0000256|HAMAP-Rule:MF_00495}.
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily.
CC CbbY/CbbZ/Gph/YieH family. {ECO:0000256|ARBA:ARBA00006171,
CC ECO:0000256|HAMAP-Rule:MF_00495}.
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DR EMBL; CP001349; ACL56296.1; -; Genomic_DNA.
DR RefSeq; WP_015927992.1; NC_011894.1.
DR AlphaFoldDB; B8IKT9; -.
DR STRING; 460265.Mnod_1296; -.
DR KEGG; mno:Mnod_1296; -.
DR eggNOG; COG0546; Bacteria.
DR HOGENOM; CLU_045011_19_1_5; -.
DR OrthoDB; 9793014at2; -.
DR UniPathway; UPA00865; UER00834.
DR Proteomes; UP000008207; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008967; F:phosphoglycolate phosphatase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0046295; P:glycolate biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR HAMAP; MF_00495; GPH_hydrolase_bact; 1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006439; HAD-SF_hydro_IA.
DR InterPro; IPR041492; HAD_2.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR023198; PGP-like_dom2.
DR InterPro; IPR037512; PGPase_prok.
DR NCBIfam; TIGR01549; HAD-SF-IA-v1; 1.
DR NCBIfam; TIGR01449; PGP_bact; 1.
DR PANTHER; PTHR43434:SF1; PHOSPHATASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_7G00760)-RELATED; 1.
DR PANTHER; PTHR43434; PHOSPHOGLYCOLATE PHOSPHATASE; 1.
DR Pfam; PF13419; HAD_2; 1.
DR SFLD; SFLDG01129; C1.5:_HAD__Beta-PGM__Phosphata; 1.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277, ECO:0000256|HAMAP-
KW Rule:MF_00495};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00495};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00495};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00495}; Reference proteome {ECO:0000313|Proteomes:UP000008207}.
FT ACT_SITE 14
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00495"
FT BINDING 14
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00495"
FT BINDING 16
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00495"
FT BINDING 176
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00495"
SQ SEQUENCE 233 AA; 24590 MW; 94E41A5C88268D6B CRC64;
MSPPLSLAPI VVFDLDGTLA ETAGDLIATL NVVLDREGLP PMDVARARDF IGAGARALIA
RGFAAAGRDL APDRLDALFR VFLAHYGQHL CVTSHLFPGA GPALDRLAAA GYRLAVCTNK
VEDHSVRLLQ LLGVADRFAA ICGRDTFPWS KPDPRHLTET IARAGGDPAR AIMVGDSRTD
IATARAAGIP AVAVPFGYTD VPVRDLGPDV IIDHFDALFD AVQHLNGLAR SAA
//
